The acceleration by polylysine of the activation of factor X by factor IXa.
The present study reports that polylysine can function as a cofactor in the conversion of factor X to factor Xa by factor IXa. In the presence of polylysine, factor X is converted to factor Xa by factor IXa as demonstrated by both clotting and amidolytic assays. The activation of factor X by factor IXa requires the prior activation of factor IX to IXa by factor XIa. Conversion of factor X to factor Xa by factor IXa is not observed in the absence of polylysine. The activation reaction proceeds optimally at pH 8.0 with an equal weight ratio of polylysine to factor X. The effect of polylysine is readily reversed by low concentrations of NaCl or elevated temperature suggesting that electrostatic interactions are of primary importance in the polylysine facilitation of the activation of factor X by factor IXa.
D000818:Animals; D001780:Blood Coagulation Tests / Q000379:methods; D002122:Calcium Chloride / Q000494:pharmacology; D002417:Cattle; D004492:Edetic Acid / Q000494:pharmacology; D005164:Factor IX; D015949:Factor IXa; D005170:Factor X; D006801:Humans; D010455:Peptides / Q000494:pharmacology*; D011107:Polylysine / Q000494:pharmacology*; D013997:Time Factors
D010455:Peptides; D011107:Polylysine; D005164:Factor IX; D005170:Factor X; D004492:Edetic Acid; D015949:Factor IXa; D002122:Calcium Chloride